| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| FRAAL1502 | FRAAL2005 | FRAAL1502 | FRAAL2005 | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.584 |
| FRAAL1502 | rlmN | FRAAL1502 | FRAAL5776 | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. | 0.406 |
| FRAAL2005 | FRAAL1502 | FRAAL2005 | FRAAL1502 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Conserved hypothetical protein; Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Belongs to the HAM1 NTPase family. | 0.584 |
| FRAAL2005 | FRAAL3253 | FRAAL2005 | FRAAL3253 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Pyruvate-flavodoxin oxidoreductase; Function of strongly homologous gene; enzyme. | 0.711 |
| FRAAL2005 | FRAAL6414 | FRAAL2005 | FRAAL6414 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Putative two-component system sensory histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.625 |
| FRAAL2005 | FRAAL6455 | FRAAL2005 | FRAAL6455 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Putative two-component system sensory histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.646 |
| FRAAL2005 | hrcA | FRAAL2005 | FRAAL2006 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Heat-inducible transcription repressor hrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.606 |
| FRAAL2005 | lepA | FRAAL2005 | FRAAL2003 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | GTP-binding elongation factor; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.724 |
| FRAAL2005 | miaB | FRAAL2005 | FRAAL5712 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Putative 2-methylthioadenine synthetase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.616 |
| FRAAL2005 | mutY | FRAAL2005 | FRAAL6530 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | A/G-specific adenine glycosylase; Function of strongly homologous gene; enzyme. | 0.571 |
| FRAAL2005 | pnp | FRAAL2005 | FRAAL5753 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Polynucleotide phosphorylase, has polyadenylase activity; Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'- direction. | 0.534 |
| FRAAL2005 | rlmN | FRAAL2005 | FRAAL5776 | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | Fe-S-cluster redox enzyme; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs; Belongs to the radical SAM superfamily. RlmN family. | 0.633 |
| FRAAL3253 | FRAAL2005 | FRAAL3253 | FRAAL2005 | Pyruvate-flavodoxin oxidoreductase; Function of strongly homologous gene; enzyme. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.711 |
| FRAAL3253 | FRAAL6414 | FRAAL3253 | FRAAL6414 | Pyruvate-flavodoxin oxidoreductase; Function of strongly homologous gene; enzyme. | Putative two-component system sensory histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.688 |
| FRAAL3253 | FRAAL6455 | FRAAL3253 | FRAAL6455 | Pyruvate-flavodoxin oxidoreductase; Function of strongly homologous gene; enzyme. | Putative two-component system sensory histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.872 |
| FRAAL3253 | miaB | FRAAL3253 | FRAAL5712 | Pyruvate-flavodoxin oxidoreductase; Function of strongly homologous gene; enzyme. | Putative 2-methylthioadenine synthetase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.474 |
| FRAAL6414 | FRAAL2005 | FRAAL6414 | FRAAL2005 | Putative two-component system sensory histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Heme chaperone HemW; Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the anaerobic coproporphyrinogen-III oxidase family. | 0.625 |
| FRAAL6414 | FRAAL3253 | FRAAL6414 | FRAAL3253 | Putative two-component system sensory histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Pyruvate-flavodoxin oxidoreductase; Function of strongly homologous gene; enzyme. | 0.688 |
| FRAAL6414 | FRAAL6455 | FRAAL6414 | FRAAL6455 | Putative two-component system sensory histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Putative two-component system sensory histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | 0.997 |
| FRAAL6414 | miaB | FRAAL6414 | FRAAL5712 | Putative two-component system sensory histidine kinase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; enzyme. | Putative 2-methylthioadenine synthetase; Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6- (dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine. | 0.419 |